Identification of
 ccdA
 in
 Paracoccus pantotrophus
 GB17: Disruption of
 ccdA
 Causes Complete Deficiency in
 c
 -Type Cytochromes

Bardischewsky, Frank; Friedrich, Cornelius G.

doi:10.1128/jb.183.1.257-263.2001

Cited by 30 publications

(29 citation statements)

References 54 publications

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“…CcdA functions in transmembrane transfer of thiol-reducing equivalents from the bacterial cytoplasm to the periplasm (Kadokura et al, 2003;Le Brun et al, 2000;Ortenberg & Beckwith 2003), and is related to the DsbD/DipZ family of membrane proteins (Kimball et al, 2003). Mutation in ccdA in other bacteria results in a deficiency in c-type cytochromes, presumably by blocking reduction of apocytochrome c thiols in the haem binding site (Bardischewsky & Friedrich 2001;Deshmukh et al, 2000). Mutant W3 (ccdA) exhibited an unexpected phenotype in lacking cytochrome aa 3 terminal oxidases in both exponential and stationary cultures.…”

Section: Discussionmentioning

confidence: 99%

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

et al. 2007

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Section: Discussionmentioning

confidence: 99%

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

et al. 2007

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“…The E. coli strains used were S17-1 (recA pro thi hsdS, RP4 tra-functions supE44) (Simon et al, 1983) and XL-1 Blue (hsdR17 recA1 endA1 gyrA46 thi relA1 lac [F9proAB, lacI q ZDM15 Tn10 (Tet r )]) (Bullock et al, 1987;Stratagene). Paracoccus pantotrophus strains used were GB17 (Sox + Hox + ) (Robertson & Kuenen, 1983;Rainey et al, 1999), GBVV (Sox 2 Hox L , V-Km interposon integrated in soxV) (Bardischewsky & Friedrich, 2001b), GBVX (Sox 2 , V-Km interposon integrated in soxX) and TP43 (Sox 2 cyt c 2 , Tn5-mob integrated in ccdA) (Chandra & Friedrich, 1986;Bardischewsky & Friedrich, 2001a). Plasmid pBHP6 carrying the soxVW genes (Bardischewsky & Friedrich, 2001b), pRIN2.6 the soxW gene, and pRIPVphoA the soxV gene (this study) were used for complementation studies.…”

Section: Methodsmentioning

confidence: 99%

“…Inactivation of ccdA of P. pantotrophus causes pleiotropic effects due to the inability to mature c-type cytochromes which are involved in different metabolic pathways such as dissimilatory nitrite reduction, and hydrogen and thiosulfate oxidation. Therefore, for CcdA of P. pantotrophus a similar role was suggested as shown for DsbD of Escherichia coli (Crooke & Cole, 1995;Bardischewsky & Friedrich, 2001a) and CcdA of Bacillus subtilis (Schiött et al, 1997), which transport reductant from the cytoplasm into the periplasm, for re-reduction of the cytochrome c apoprotein, an essential step for binding of the haem moiety.…”

Section: Introductionmentioning

confidence: 99%

“…SoxV predicts a protein with six transmembrane helices which is closely related with respect to its primary and secondary structure to CcdA of P. pantotrophus and other bacteria involved in cytochrome c biogenesis (Bardischewsky & Friedrich, 2001a). SoxW predicts a periplasmic protein with characteristics of members of the thioredoxin superfamily (Bardischewsky & Friedrich, 2001b).…”

Section: Introductionmentioning

confidence: 99%

“…In P. pantotrophus the soxVWXYZABCDEFGH genes constitute two transcriptional units, soxVW and soxX-H (Rother et al, 2005). In the homogenote mutant GBVV carrying the soxV : : V-kanamycin interposon soxX-H are expressed upon growth with thiosulfate as in the wild-type GB17 (Bardischewsky & Friedrich, 2001b).SoxV predicts a protein with six transmembrane helices which is closely related with respect to its primary and secondary structure to CcdA of P. pantotrophus and other bacteria involved in cytochrome c biogenesis (Bardischewsky & Friedrich, 2001a). SoxW predicts a periplasmic protein with characteristics of members of the thioredoxin superfamily (Bardischewsky & Friedrich, 2001b).…”

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SoxV transfers electrons to the periplasm of Paracoccus pantotrophus – an essential reaction for chemotrophic sulfur oxidation

et al. 2006

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The soxVW genes are located upstream of the sox gene cluster encoding the sulfur-oxidizing ability of Paracoccus pantotrophus. SoxV is highly homologous to CcdA, which is involved in cytochrome c maturation of P. pantotrophus. SoxV was shown to function in reduction of the periplasmic SoxW, which shows a CysXaaXaaCys motif characteristic for thioredoxins. From strain GBVV, which carries an V-kanamycin-resistance-encoding interposon in soxV, and complementation analysis it was evident that SoxV but not the periplasmic SoxW was essential for lithoautotrophic growth of P. pantotrophus with thiosulfate. However, the thiosulfate-oxidizing activities of cell extracts from the wild-type and from strain GBVV were similar, demonstrating that the low thiosulfate-oxidizing activity of strain GBVV in vivo was not due to a defect in biosynthesis or maturation of proteins of the Sox system and suggesting that SoxV is part of a regulatory or catalytic system of the Sox system. Analysis of DNA sequences available from different organisms harbouring a Sox system revealed that soxVW genes are exclusively present in sox operons harbouring the soxCD genes, encoding sulfur dehydrogenase, suggesting that SoxCD might be a redox partner of SoxV. No complementation of the ccdA mutant P. pantotrophus TP43 defective in cytochrome c maturation was achieved by expression of soxV in trans, demonstrating that the high identity of SoxV and CcdA does not correspond to functional homology. INTRODUCTIONThe reversible formation of protein-disulfide bonds plays an important role in transport of electrons, protein biogenesis, protein stability and enzyme catalysis (Akyama & Ito, 1993;Yamanaka et al., 1994;Okamoto et al., 1995;Missiakis & Raina, 1997; reviewed by Fabianek et al., 2000;Ritz & Beckwith, 2001). Different thiol : disulfide oxidoreductases have been identified which are involved in the formation, isomerization and reduction of disulfide bonds in different bacteria. All these oxidoreductases share a conserved CysXaaXaaCys motif and a common tertiary structure known as the thioredoxin-like fold (Martin, 1995). Members of the DsbD and CcdA families are involved in the transport of electrons from the cytoplasm to the periplasm for reduction of apocytochromes to enable addition of the haem moiety (reviewed by Thöny-Meyer, 1997). The electrons are transferred from a cytoplasmic thioredoxin first to the central transmembrane b-domain of DsbD then to the Cterminal thioredoxin-like c-domain and therefrom to the N-terminal a-domain, which then reduces either DsbC or CcmG (Rietsch et al., 1997;Stewart et al., 1999;Chung et al., 2000;Katzen & Beckwith, 2000).The Gram-negative, facultatively chemolithoautotrophic bacterium Paracoccus pantotrophus grows under aerobic conditions lithotrophically with molecular hydrogen and thiosulfate as energy source for autotrophic carbon dioxide fixation (Robertson & Kuenen, 1983;Rainey et al., 1999). In P. pantotrophus the soxVWXYZABCDEFGH genes constitute two transcriptional units, soxVW and soxX-H (Rother et al., ...

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An Overview of the Biochemical and Molecular Aspects of Microbial Oxidation of Inorganic Sulfur Compounds

Mohapatra¹,

Gould

Dinardo

et al. 2008

CLEAN Soil Air Water

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Inorganic sulfur compounds are oxidized mostly to sulfate by microorganisms belonging to the bacteria and archaea domains. These microorganisms produce different types of enzymes, e. g., oxidoreductases and hydrolases for the metabolism of inorganic sulfur compounds. These versatile biocatalysts have potential biotechnological applications in different fields including biohydrometallurgical processes for recovering precious heavy metals and also for bioremediation of sulfides in industrial waste effluents. Appropriate knowledge on the enzymatic pathways of inorganic sulfur compounds oxidation will help to tailor the catalytic properties of these microorganisms so that they are optimal not only for a given reaction but also in the context of harsh industrial processes. This review describes the distribution of inorganic sulfur compound-oxidizing microorganisms, various enzymatic systems associated with sulfur metabolism, and identification of the gene(s) responsible for catalysis of different enzymatic reactions.

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Identification of ccdA in Paracoccus pantotrophus GB17: Disruption of ccdA Causes Complete Deficiency in c -Type Cytochromes

Cited by 30 publications

References 54 publications

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

SoxV transfers electrons to the periplasm of Paracoccus pantotrophus – an essential reaction for chemotrophic sulfur oxidation

An Overview of the Biochemical and Molecular Aspects of Microbial Oxidation of Inorganic Sulfur Compounds

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